Biochemistry 2280A Chapter Notes - Chapter 2: Competitive Inhibition, Allosteric Regulation, Conformational Change
Document Summary
Induce conformational change in enzyme that promotes its activity: prosthetic groups -> tightly bound cofactors or coenzymes that are necessary for enzyme function. 2. 3 enzyme kinetics: kinetics of monomeric enzymes, enzymes experience saturation kinetics, as substrate [] increases, reaction rate increases until max value is reached. Increase [s: when starts low -> increase cause increase in enzyme activity. If high -> increasing has no effect since vmax has been attained. Increase [e: will always increase vmax regardless of starting [, michaelis-menten, when reaction rate = vmax/2 -> km = [s, hyperbola relationship between [s] and reaction velocity, v vs. [s] 2. 4 effects of local conditions on enzyme activity: temperature, t enzyme activity , above body t -> enzyme activity quickly drops off as enzyme denatures, ph, enzymes are max active within small ph range. If outside -> activity drops w/ changes in ph as ionization of active site changes.